Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.UniRule annotation

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.UniRule annotation
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2Schiff-base intermediate with DNAUniRule annotation1
Active sitei3Proton donorUniRule annotation1
Active sitei57Proton donor; for beta-elimination activityUniRule annotation1
Binding sitei90DNAUniRule annotation1
Binding sitei109DNAUniRule annotation1
Binding sitei150DNAUniRule annotation1
Active sitei259Proton donor; for delta-elimination activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-typeUniRule annotationAdd BLAST35

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Glycosidase, Hydrolase, Lyase, Multifunctional enzyme
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciVPAR223926:G1GTB-200-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Formamidopyrimidine-DNA glycosylaseUniRule annotation (EC:3.2.2.23UniRule annotation)
Short name:
Fapy-DNA glycosylaseUniRule annotation
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutMUniRule annotation (EC:4.2.99.18UniRule annotation)
Short name:
AP lyase MutMUniRule annotation
Gene namesi
Name:mutMUniRule annotation
Synonyms:fpgUniRule annotation
Ordered Locus Names:VP0189
OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic identifieri223926 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000002493 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001708832 – 269Formamidopyrimidine-DNA glycosylaseAdd BLAST268

Proteomic databases

PRIDEiQ87T81

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi223926.VP0189

Structurei

3D structure databases

ProteinModelPortaliQ87T81
SMRiQ87T81
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-typeUniRule annotationAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020881
KOiK10563
OMAiRNSRLRW

Family and domain databases

Gene3Di3.20.190.10, 1 hit
HAMAPiMF_00103 Fapy_DNA_glycosyl, 1 hit
InterProiView protein in InterPro
IPR015886 DNA_glyclase/AP_lyase_DNA-bd
IPR015887 DNA_glyclase_Znf_dom_DNA_BS
IPR020629 Formamido-pyr_DNA_Glyclase
IPR012319 FPG_cat
IPR035937 MutM-like_N-ter
IPR010979 Ribosomal_S13-like_H2TH
IPR000214 Znf_DNA_glyclase/AP_lyase
IPR010663 Znf_FPG/IleRS
PfamiView protein in Pfam
PF01149 Fapy_DNA_glyco, 1 hit
PF06831 H2TH, 1 hit
PF06827 zf-FPG_IleRS, 1 hit
SMARTiView protein in SMART
SM00898 Fapy_DNA_glyco, 1 hit
SM01232 H2TH, 1 hit
SUPFAMiSSF46946 SSF46946, 1 hit
SSF81624 SSF81624, 1 hit
TIGRFAMsiTIGR00577 fpg, 1 hit
PROSITEiView protein in PROSITE
PS51068 FPG_CAT, 1 hit
PS01242 ZF_FPG_1, 1 hit
PS51066 ZF_FPG_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q87T81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVEVS RMGISPHMVG QTIKAFVFRT PKLRWDIPQE LKLLEGQVIR
60 70 80 90 100
NIRRRAKYLL IDTDQGTAIV HLGMSGSLRV LDADFPAAKH DHVDLKLTNG
110 120 130 140 150
KVLRYNDPRR FGAWLWCAPG ESHAVLEHMG PEPLTDAFNS EYIADKAQGK
160 170 180 190 200
RVAVKQFIMD NKVVVGVGNI YANESLFKSR ILPTRQAGQV TPQEWVLLVE
210 220 230 240 250
NIKATLKIAI NQGGTTLKDF AQADGKPGYF AQELLVYGKA GEPCPECGEP
260
LQELKIGQRN TFFCNECQQ
Length:269
Mass (Da):30,096
Last modified:January 23, 2007 - v3
Checksum:i77A1CB9CEF07E8C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000031 Genomic DNA Translation: BAC58452.1
RefSeqiNP_796568.1, NC_004603.1
WP_005462495.1, NC_004603.1

Genome annotation databases

EnsemblBacteriaiBAC58452; BAC58452; BAC58452
GeneIDi1187656
KEGGivpa:VP0189
PATRICifig|223926.6.peg.181

Similar proteinsi

Entry informationi

Entry nameiFPG_VIBPA
AccessioniPrimary (citable) accession number: Q87T81
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 103 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health